Q64520 (KGUA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanylate kinase
EC=2.7.4.8

Alternative name(s):
GMP kinase

Gene names

Name:	Guk1
Synonyms:	Gmk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for recycling GMP and indirectly, cGMP.
Catalytic activity	ATP + GMP = ADP + GDP.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the guanylate kinase family. Contains 1 guanylate kinase-like domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	purine nucleotide metabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW guanylate kinase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 198

197

Guanylate kinase

PRO_0000170652

Regions

Domain

4 – 186

183

Guanylate kinase-like

Nucleotide binding

11 – 18

8

ATP

Sites

Active site

44

1

Probable

Active site

137

1

Probable

Active site

148

1

Probable

Binding site

171

1

ATP

Binding site

172

1

ATP; via carbonyl oxygen

Amino acid modifications

Modified residue

53

1

Phosphotyrosine Ref.3

Secondary structure

1

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198

Helix Strand Turn

Details...

Beta strand

7 – 10

4

Helix

17 – 28

12

Turn

29 – 31

3

Beta strand

32 – 34

3

Turn

49 – 51

3

Helix

58 – 67

10

Beta strand

70 – 76

7

Beta strand

79 – 84

6

Helix

85 – 93

9

Beta strand

97 – 101

5

Helix

104 – 110

7

Beta strand

118 – 123

6

Helix

127 – 137

11

Helix

142 – 155

14

Helix

156 – 160

5

Turn

162 – 164

3

Beta strand

166 – 170

5

Helix

174 – 184

11

Helix

186 – 191

6

Sequences

	Sequence		Length	Mass (Da)
	Q64520 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F584E4B6521C607B	FASTA	198	21,918
	10 20 30 40 50 60 MAGPRPVVLS GPSGAGKSTL LKKLFQEHSS IFGFSVSHTT RNPRPGEEDG KDYYFVTREM 70 80 90 100 110 120 MQRDIAAGDF IEHAEFSGNL YGTSKEAVRA VQAMNRICVL DVDLQGVRSI KKTDLCPIYI 130 140 150 160 170 180 FVQPPSLDVL EQRLRLRNTE TEESLAKRLA AARTDMESSK EPGLFDLVII NDDLDKAYAT 190 LKQALSEEIK KAQGTGHA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, characterization, and modeling of mouse and human guanylate kinases." Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E. J. Biol. Chem. 271:16734-16740(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[3]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53, MASS SPECTROMETRY. Tissue: Brain.
[4]	"Structural characterization of the closed conformation of mouse guanylate kinase." Sekulic N., Shuvalova L., Spangenberg O., Konrad M., Lavie A. J. Biol. Chem. 277:30236-30243(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), ATP-BINDING SITES, ACTIVE SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U53514 mRNA. Translation: AAC52652.1.
BC024625 mRNA. Translation: AAH24625.1.

IPI

IPI00986878.

UniGene

Mm.3624.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LVG	X-ray	2.10	A	1-198	[»]

ProteinModelPortal

Q64520.

SMR

Q64520. Positions 5-194.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q64520. 1 interaction.

PTM databases

PhosphoSite

Q64520.

Proteomic databases

PaxDb

Q64520.

PRIDE

Q64520.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

MGI

MGI:95871. Guk1.

Phylogenomic databases

eggNOG

COG0194.

HOVERGEN

HBG003344.

InParanoid

Q64520.

OrthoDB

EOG4NS3CS.

Gene expression databases

ArrayExpress

Q64520.

Bgee

Q64520.

CleanEx

MM_GUK1.

Genevestigator

Q64520.

GermOnline

ENSMUSG00000020444. Mus musculus.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR017665. Guanylate_kinase_sub.
[Graphical view]

Pfam

PF00625. Guanylate_kin. 1 hit.
[Graphical view]

SMART

SM00072. GuKc. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03263. guanyl_kin. 1 hit.

PROSITE

PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GUK1. mouse.

EvolutionaryTrace

Q64520.

SOURCE

Search...

Entry information

Entry name

KGUA_MOUSE

Accession

Primary (citable) accession number: Q64520

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program